Lectins in the Rock Lobster Jasus Novaehollandiae Hemolymph

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Hcmolymph of three different species of rock lobsters was examined for its agglutinating activity using mammalian erythrocytes and bacteria. The hemolymph of the red rock lobster Jasus novaehollandiae agglutinated human ABO erythrocytes and also a marine bacterium Pseudomonas aeruginosa. The hemagglutinating activity was, however, inconsistent, and varied from a titer of 4 to 1024 for human erythrocytes. J. novaehollandiae lectins were heat-labile and the hemagglutinating activity was dependent on the presence of Ca2+. The major lectin named JN-2 was a glycoprotein having a molecular weight of 400,000 and dissociated into subunits of different molecular sizes (85, 81, and 63kD). Porcine stomach mucin (PSM), asialo-PSM, and fetuin were effective inhibitors to J. novaehollandiae lectins. N-acetylneuraminic acid did not inhibit the hemagglutinating activity. Simple sugars such as D-ribose, D-arabinose, and D-galactose also inhibited the hemagglutinating activity to some extent. Another species of the red rock lobster J. edwardsii was found to possess lectins similar to those of J. novaehollandiae. On the contrary, the humoral lectin(s) of the green rock lobster J. verreauxi was sialic acid-specific, and the lectin activity was independent of the presence of Ca2+.